5B23

X-ray Structure of Clostridium Perfringens Sortase B

5B23 の概要

• エントリーDOI: 10.2210/pdb5b23/pdb
• 分子名称: Uncharacterized protein Sortase B (2 entities in total)
• 機能のキーワード: transpeptidase, sortase, clostridium perfringens, hydrolase
• 由来する生物種: Clostridium perfringens (strain 13 / Type A)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55581.51

構造登録者

Kamitori, S.,Yoshida, H.,Tamai, E. (登録日: 2015-12-28, 公開日: 2016-12-28, 最終更新日: 2023-11-08)

主引用文献

Tamai, E.,Sekiya, H.,Maki, J.,Nariya, H.,Yoshida, H.,Kamitori, S.
X-ray structure of Clostridium perfringens sortase B cysteine transpeptidase
Biochem. Biophys. Res. Commun., 493:1264-1272, 2017

PubMed Abstract: The pathogenesis and infectivity of Gram-positive bacteria are mediated by many surface proteins that are covalently attached to peptidoglycans of the cell wall. The covalent attachment of these proteins is catalyzed by sortases (Srts), a family of cysteine transpeptidases, which are classified into six classes, A - F, based on their amino acid sequences and biological roles. Clostridium perfringens, one of the pathogenic clostridial species, has a class B sortase (CpSrtB) with 249 amino acid residues. X-ray structures of CpSrtB and its inactive mutant form were determined at 2.2 Å and 1.8 Å resolutions, respectively. CpSrtB adopts a typical sortase-protein fold, and has a unique substrate-binding groove formed by three β-strands and two helices creating the sidewalls of the groove. The position of the catalytic Cys232 of CpSrtB is significantly different from those commonly found in Srts structures. The modeling study of the CpSrtB/peptide complex suggested that the position of Cys232 found in CpSrtB is preferable for the catalytic reaction to occur. Structural comparison with other class B sortases demonstrated that the catalytic site likely converts between two forms. The movement of Cys232 between the two forms may help His136 deprotonate Cys232 to be activated as a thiolate, which may the catalytic Cys-activated mechanism for Srts.

PubMed: 28962862
DOI: 10.1016/j.bbrc.2017.09.144

実験手法

X-RAY DIFFRACTION (2.2 Å)